KRE2_YEAST
ID KRE2_YEAST Reviewed; 442 AA.
AC P27809; D6VTA6;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 1.
DT 03-AUG-2022, entry version 195.
DE RecName: Full=Glycolipid 2-alpha-mannosyltransferase;
DE EC=2.4.1.-;
DE AltName: Full=Alpha-1,2-mannosyltransferase;
GN Name=KRE2; Synonyms=MNT1; OrderedLocusNames=YDR483W; ORFNames=D8035.26;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE, AND
RP GLYCOSYLATION AT ASN-197.
RX PubMed=1550992; DOI=10.1093/glycob/2.1.77;
RA Haeusler A., Robbins P.W.;
RT "Glycosylation in Saccharomyces cerevisiae: cloning and characterization of
RT an alpha-1,2-mannosyltransferase structural gene.";
RL Glycobiology 2:77-84(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1541391; DOI=10.1093/genetics/130.2.273;
RA Hill K., Boone C., Goebl M., Puccia R., Sdicu A.-M., Bussey H.;
RT "Yeast KRE2 defines a new gene family encoding probable secretory proteins,
RT and is required for the correct N-glycosylation of proteins.";
RL Genetics 130:273-283(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(1997).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 101-442.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7754710; DOI=10.1002/yea.320100909;
RA Koelling R., Lee A., Chen E.Y., Botstein D.;
RT "Nucleotide sequence of the SAC2 gene of Saccharomyces cerevisiae.";
RL Yeast 10:1211-1216(1994).
RN [6]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
CC -!- FUNCTION: Mannosyltransferase that transfers an alpha-D-mannosyl
CC residue from GDP-mannose into lipid-linked oligosaccharide, forming an
CC alpha-(1->2)-D-mannosyl-D-mannose linkage. Required for the attachment
CC of the third mannose residue of O-linked saccharides.
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane; Single-pass type II
CC membrane protein.
CC -!- MISCELLANEOUS: Present with 13000 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 15 family.
CC {ECO:0000305}.
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DR EMBL; M81110; AAA34784.1; -; Genomic_DNA.
DR EMBL; X62647; CAA44516.1; -; Genomic_DNA.
DR EMBL; U33050; AAB64906.1; -; Genomic_DNA.
DR EMBL; Z29988; CAA82879.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA12316.1; -; Genomic_DNA.
DR PIR; S32592; S32592.
DR RefSeq; NP_010771.1; NM_001180791.1.
DR PDB; 1S4N; X-ray; 2.01 A; A/B=97-442.
DR PDB; 1S4O; X-ray; 2.01 A; A/B=97-442.
DR PDB; 1S4P; X-ray; 2.01 A; A/B=97-442.
DR PDBsum; 1S4N; -.
DR PDBsum; 1S4O; -.
DR PDBsum; 1S4P; -.
DR AlphaFoldDB; P27809; -.
DR SMR; P27809; -.
DR BioGRID; 32535; 57.
DR DIP; DIP-5373N; -.
DR IntAct; P27809; 11.
DR STRING; 4932.YDR483W; -.
DR CAZy; GT15; Glycosyltransferase Family 15.
DR iPTMnet; P27809; -.
DR MaxQB; P27809; -.
DR PaxDb; P27809; -.
DR PRIDE; P27809; -.
DR EnsemblFungi; YDR483W_mRNA; YDR483W; YDR483W.
DR GeneID; 852094; -.
DR KEGG; sce:YDR483W; -.
DR SGD; S000002891; KRE2.
DR VEuPathDB; FungiDB:YDR483W; -.
DR eggNOG; KOG4472; Eukaryota.
DR GeneTree; ENSGT00940000176287; -.
DR HOGENOM; CLU_024327_1_0_1; -.
DR InParanoid; P27809; -.
DR OMA; FMQMNNK; -.
DR BioCyc; MetaCyc:G3O-30008-MON; -.
DR BioCyc; YEAST:G3O-30008-MON; -.
DR UniPathway; UPA00378; -.
DR EvolutionaryTrace; P27809; -.
DR PRO; PR:P27809; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; P27809; protein.
DR GO; GO:0000329; C:fungal-type vacuole membrane; HDA:SGD.
DR GO; GO:0005794; C:Golgi apparatus; IDA:SGD.
DR GO; GO:0005797; C:Golgi medial cisterna; IDA:CACAO.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0000026; F:alpha-1,2-mannosyltransferase activity; IDA:SGD.
DR GO; GO:0000032; P:cell wall mannoprotein biosynthetic process; IMP:SGD.
DR GO; GO:0097502; P:mannosylation; IBA:GO_Central.
DR GO; GO:0006491; P:N-glycan processing; IMP:SGD.
DR GO; GO:0006487; P:protein N-linked glycosylation; IBA:GO_Central.
DR GO; GO:0006493; P:protein O-linked glycosylation; IMP:SGD.
DR Gene3D; 3.90.550.10; -; 1.
DR InterPro; IPR002685; Glyco_trans_15.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR PANTHER; PTHR31121; PTHR31121; 1.
DR Pfam; PF01793; Glyco_transf_15; 1.
DR PIRSF; PIRSF018153; Glyco_trans_15; 1.
DR SUPFAM; SSF53448; SSF53448; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Glycoprotein; Glycosyltransferase;
KW Golgi apparatus; Manganese; Membrane; Reference proteome; Signal-anchor;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..442
FT /note="Glycolipid 2-alpha-mannosyltransferase"
FT /id="PRO_0000208241"
FT TOPO_DOM 1..11
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 12..30
FT /note="Helical; Signal-anchor for type II membrane protein"
FT TOPO_DOM 31..442
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 31..118
FT /note="Stem region"
FT REGION 68..95
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 119..442
FT /note="Catalytic"
FT ACT_SITE 329
FT /note="Nucleophile"
FT /evidence="ECO:0000255"
FT CARBOHYD 197
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:1550992"
FT HELIX 106..110
FT /evidence="ECO:0007829|PDB:1S4N"
FT HELIX 111..113
FT /evidence="ECO:0007829|PDB:1S4N"
FT STRAND 123..128
FT /evidence="ECO:0007829|PDB:1S4N"
FT HELIX 131..133
FT /evidence="ECO:0007829|PDB:1S4N"
FT HELIX 134..147
FT /evidence="ECO:0007829|PDB:1S4N"
FT TURN 148..151
FT /evidence="ECO:0007829|PDB:1S4N"
FT STRAND 156..162
FT /evidence="ECO:0007829|PDB:1S4N"
FT HELIX 166..175
FT /evidence="ECO:0007829|PDB:1S4N"
FT STRAND 180..184
FT /evidence="ECO:0007829|PDB:1S4N"
FT HELIX 187..189
FT /evidence="ECO:0007829|PDB:1S4N"
FT HELIX 198..208
FT /evidence="ECO:0007829|PDB:1S4N"
FT TURN 209..211
FT /evidence="ECO:0007829|PDB:1S4N"
FT TURN 213..216
FT /evidence="ECO:0007829|PDB:1S4N"
FT HELIX 218..229
FT /evidence="ECO:0007829|PDB:1S4N"
FT HELIX 231..233
FT /evidence="ECO:0007829|PDB:1S4N"
FT HELIX 235..237
FT /evidence="ECO:0007829|PDB:1S4N"
FT STRAND 241..245
FT /evidence="ECO:0007829|PDB:1S4N"
FT HELIX 260..266
FT /evidence="ECO:0007829|PDB:1S4N"
FT STRAND 271..274
FT /evidence="ECO:0007829|PDB:1S4N"
FT STRAND 276..278
FT /evidence="ECO:0007829|PDB:1S4N"
FT HELIX 281..283
FT /evidence="ECO:0007829|PDB:1S4N"
FT HELIX 287..297
FT /evidence="ECO:0007829|PDB:1S4N"
FT HELIX 299..301
FT /evidence="ECO:0007829|PDB:1S4N"
FT HELIX 308..311
FT /evidence="ECO:0007829|PDB:1S4N"
FT STRAND 322..324
FT /evidence="ECO:0007829|PDB:1S4N"
FT STRAND 328..332
FT /evidence="ECO:0007829|PDB:1S4N"
FT HELIX 333..336
FT /evidence="ECO:0007829|PDB:1S4N"
FT HELIX 339..351
FT /evidence="ECO:0007829|PDB:1S4N"
FT HELIX 353..356
FT /evidence="ECO:0007829|PDB:1S4N"
FT HELIX 361..372
FT /evidence="ECO:0007829|PDB:1S4N"
FT HELIX 375..377
FT /evidence="ECO:0007829|PDB:1S4N"
FT STRAND 378..380
FT /evidence="ECO:0007829|PDB:1S4N"
FT STRAND 386..388
FT /evidence="ECO:0007829|PDB:1S4N"
FT STRAND 391..393
FT /evidence="ECO:0007829|PDB:1S4N"
FT HELIX 398..403
FT /evidence="ECO:0007829|PDB:1S4N"
FT HELIX 410..412
FT /evidence="ECO:0007829|PDB:1S4N"
FT HELIX 422..429
FT /evidence="ECO:0007829|PDB:1S4N"
FT HELIX 437..441
FT /evidence="ECO:0007829|PDB:1S4N"
SQ SEQUENCE 442 AA; 51387 MW; E2A54786F8C8AA60 CRC64;
MALFLSKRLL RFTVIAGAVI VLLLTLNSNS RTQQYIPSSI SAAFDFTSGS ISPEQQVISE
ENDAKKLEQS ALNSEASEDS EAMDEESKAL KAAAEKADAP IDTKTTMDYI TPSFANKAGK
PKACYVTLVR NKELKGLLSS IKYVENKINK KFPYPWVFLN DEPFTEEFKE AVTKAVSSEV
KFGILPKEHW SYPEWINQTK AAEIRADAAT KYIYGGSESY RHMCRYQSGF FWRHELLEEY
DWYWRVEPDI KLYCDINYDV FKWMQENEKV YGFTVSIHEY EVTIPTLWQT SMDFIKKNPE
YLDENNLMSF LSNDNGKTYN LCHFWSNFEI ANLNLWRSPA YREYFDTLDH QGGFFYERWG
DAPVHSIAAA LFLPKDKIHY FSDIGYHHPP YDNCPLDKEV YNSNNCECDQ GNDFTFQGYS
CGKEYYDAQG LVKPKNWKKF RE
